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Different evolutionary patterns of hypoxia-inducible factor ? (HIF-?) isoforms in the basal branches of Actinopterygii and Sarcopterygii.

ABSTRACT: Hypoxia-inducible factor (HIF) is a crucial regulator of cellular and systemic responses to low oxygen levels. Here we firstly cloned three HIF-? isoforms from the basal branches of Osteichthyes and used computational tools to characterise the molecular change underlying the functional divergence of HIF-? isoforms in different lineages. Only the HIF-1? and HIF-2? in African lungfish and amphibians were found under positive selection. HIF-1? and -2? were less functionally divergent in basal ray-finned fish than in teleosts, and showed conserved but different transcriptional activity towards specific target genes.

SUBMITTER: Chi W

PROVIDER: S-EPMC3836196 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Different evolutionary patterns of hypoxia-inducible factor α (HIF-α) isoforms in the basal branches of Actinopterygii and Sarcopterygii.

Chi Wei W Gan Xiaoni X Xiao Wuhan W Wang Wen W He Shunping S

FEBS open bio 20130919

Hypoxia-inducible factor (HIF) is a crucial regulator of cellular and systemic responses to low oxygen levels. Here we firstly cloned three HIF-α isoforms from the basal branches of Osteichthyes and used computational tools to characterise the molecular change underlying the functional divergence of HIF-α isoforms in different lineages. Only the HIF-1α and HIF-2α in African lungfish and amphibians were found under positive selection. HIF-1α and -2α were less functionally divergent in basal ray-f ...[more]

PMID: 24265980

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Project description:Oxygen homeostasis is crucial for development, survival and normal function of all metazoans. A family of transcription factors called hypoxia-inducible factors (HIF) is critical in mediating the adaptive responses to reduced oxygen availability. The HIF transcription factor consists of a constitutively expressed β subunit and an oxygen-dependent α subunit; the abundance of the latter determines the activity of HIF and is regulated by a family of O(2)- and Fe(2+)-dependent enzymes prolyl hydroxylases (PHDs). Currently very little is known about the function of this important pathway and the molecular structure of its key players in hypoxia-tolerant intertidal mollusks including oysters, which are among the animal champions of anoxic and hypoxic tolerance and thus can serve as excellent models to study the role of HIF cascade in adaptations to oxygen deficiency. We have isolated transcripts of two key components of the oxygen sensing pathway - the oxygen-regulated HIF-α subunit and PHD - from an intertidal mollusk, the eastern oyster Crassostrea virginica, and determined the transcriptional responses of these two genes to anoxia, hypoxia and cadmium (Cd) stress. HIF-α and PHD homologs from eastern oysters C. virginica show significant sequence similarity and share key functional domains with the earlier described isoforms from vertebrates and invertebrates. Phylogenetic analysis shows that genetic diversification of HIF and PHD isoforms occurred within the vertebrate lineage indicating functional diversification and specialization of the oxygen-sensing pathways in this group, which parallels situation observed for many other important genes. HIF-α and PHD homologs are broadly expressed at the mRNA level in different oyster tissues and show transcriptional responses to prolonged hypoxia in the gills consistent with their putative role in oxygen sensing and the adaptive response to hypoxia. Similarity in amino acid sequence, domain structure and transcriptional responses between HIF-α and PHD homologs from oysters and other invertebrate and vertebrate species implies the highly conserved functions of these genes throughout the evolutionary history of animals, in accordance with their critical role in oxygen sensing and homeostasis.

Dataset Information

Different evolutionary patterns of hypoxia-inducible factor ? (HIF-?) isoforms in the basal branches of Actinopterygii and Sarcopterygii.

Publications

Different evolutionary patterns of hypoxia-inducible factor α (HIF-α) isoforms in the basal branches of Actinopterygii and Sarcopterygii.

Similar Datasets

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